P54741 (AFSK_STRCO) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Serine/threonine-protein kinase AfsK
EC=2.7.11.1

Gene names

Name:	afsK
Ordered Locus Names:	SCO4423
ORF Names:	SC6F11.21, SCD6.01

Organism

Streptomyces coelicolor (strain ATCC BAA-471 / A3(2) / M145) [Reference proteome] [HAMAP]

Taxonomic identifier

100226 [NCBI]

Taxonomic lineage

cellular organisms › Bacteria › Actinobacteria › Actinobacteria › Actinobacteridae › Actinomycetales › Streptomycineae › Streptomycetaceae › Streptomyces › Streptomyces coelicolor

Protein attributes

Sequence length	799 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Involved in the regulation of secondary metabolism by phosphorylating, on both Ser and Thr, the AfsR global regulatory protein involved in the control of secondary metabolism.
Catalytic activity	ATP + a protein = ADP + a phosphoprotein.
Subunit structure	Interacts (via the N-terminal kinase domain) with KbpA; the interaction prevents autophosphorylation of AfsK. Ref.5
Post-translational modification	Autophosphorylated mainly on threonine residues. Some phosphorylation on serine residues. Autophosphorylation on Thr-168 is the major site enhancing kinase activity towards AfsR, and is regulated though interaction with KbpA. Ref.5 Ref.6
Sequence similarities	Belongs to the protein kinase superfamily. Ser/Thr protein kinase family. Contains 1 protein kinase domain.
Mass spectrometry	Molecular mass is 1638.8 Da from positions 68 - 93. Determined by ESI. Ref.6 Molecular mass is 1718.8 Da from positions 68 - 93. Determined by ESI. Monophosphorylated. Ref.6 Molecular mass is 2236.5 Da from positions 117 - 137. Determined by ESI. Ref.6 Molecular mass is 2109.4 Da from positions 167 - 186. Determined by ESI. Ref.6 Molecular mass is 2189.4 Da from positions 167 - 186. Determined by ESI. Monophosphorylated. Ref.6

Ontologies

Keywords
Ligand	ATP-binding Nucleotide-binding
Molecular function	Kinase Serine/threonine-protein kinase Transferase
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW protein serine/threonine kinase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 799	799	Serine/threonine-protein kinase AfsK		PRO_0000171234
Regions
	Domain	16 – 271	256	Protein kinase
	Nucleotide binding	22 – 30	9	ATP By similarity
	Compositional bias	317 – 428	112	Pro-rich
Sites
	Active site	138	1	Proton acceptor By similarity
	Binding site	44	1	ATP By similarity
Amino acid modifications
	Modified residue	71	1	Phosphoserine; by autocatalysis Ref.6
	Modified residue	168	1	Phosphothreonine; by autocatalysis Ref.6
Experimental info
	Mutagenesis	44	1	K → A: No autophosphorylation. Binds KbpA. Ref.5
	Mutagenesis	71	1	S → A: No autophosphorylation. Ref.6
	Mutagenesis	128	1	S → A: No change in autophosphorylation. Ref.6
	Mutagenesis	168	1	T → A: Almost completely abolishes autophosphorylation. No enhancement of kinase activity on AfsR. Very little constitutive kinase activity. Ref.6
	Mutagenesis	168	1	T → D: Almost completely abolishes autophosphorylation. No enhancement of kinase activity on AfsR. Constitutive kinase activity. Ref.6
	Mutagenesis	168	1	T → E: Almost completely abolishes autophosphorylation. No enhancement of kinase activity on AfsR. Some constitutive kinase activity. Ref.6
	Mutagenesis	170	1	T → D: No change in autophosphorylation. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	P54741 [UniParc]. Last modified August 14, 2001. Version 2. Checksum: 4BE9BED4169F6F5B	FASTA	799	83,788
	10 20 30 40 50 60 MVDQLTQHDP RRIGPFEVLG RLGAGGMGLV YLARSASGRR VAIKTVRTEL AEDQLFRVRF 70 80 90 100 110 120 TREVEAARAV SGFYTAAVVD ADPRAAVPWL ATAYVPAPSL EEIVNECGPM PAQAVRWLAA 130 140 150 160 170 180 GVAEALQSIH GAGLVHRDLK PSNVLVVEDG PRVIDFGIAS GVSNTRLTMT NVAVGTPAYM 190 200 210 220 230 240 SPEQAKDSRS VTGASDVFSL GSMLVFAATG HPPFHGANPV ETVFMLLREG PDLEGLPDEL 250 260 270 280 290 300 RPLIESCMQM EATGRPNPAD LQAQLAPHLF GSGSDDSGTA SAWLPERAVG LIEGRRNGRP 310 320 330 340 350 360 AVKPATTAGG RGHGHGPSGA RAPVHAPPLP PPPAHDPVVP APPAHVPAVP APVGAPDGGP 370 380 390 400 410 420 VRLPGAAVPI GPGPRVADMR AAAVAAPPPE SALAASWSRP RPGVNGADPA VPAPAPAPPE 430 440 450 460 470 480 ASPAGWRPWR FRMSNDVWGT PRVAEDLVYV TSFEVHALDV ATGRRRFKTR DVAWSMAVAD 490 500 510 520 530 540 GRIHASDGPT LFALDAREGA DLWRVQTDAW VYSLQADRGT VLTATRGGGV QAWEASAGQK 550 560 570 580 590 600 LWEVTGAQTD FESPEAGAAL HDGTAYVWQD ARLRALDART GDERWSYPIG DAASCGGVPV 610 620 630 640 650 660 RLTQAPDGYV YVAAGTRVLA LEVASGHVRW HFEAPAVFLA PPTFVPGPAV TGGGVYLADY 670 680 690 700 710 720 LGTVYALDAT DGRDRWRIAT EARSSTDPVL VAAGHVHVGS GKGLYTLDAV TGTPKWRFQA 730 740 750 760 770 780 GGDIVGAPAV AEGRIHFGSS DHLLYTLKAD DGRLRWKLAT GGEITGSPVV RDGIVYACSK 790 DRCVYALDAE KGTGTARTT

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Phosphorylation of the AfsR protein involved in secondary metabolism in Streptomyces species by a eukaryotic-type protein kinase." Matsumoto A., Hong S.K., Ishizuka H., Horinouchi S., Beppu T. Gene 146:47-56(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: A3(2) / NRRL B-16638.
[2]	"The aerial mycelium-defective phenotype of Streptomyces griseus resulting from A-factor deficiency is suppressed by a Ser/Thr kinase of S. coelicolor A3(2)." Ueda K., Umeyama T., Beppu T., Horinouchi S. Gene 169:91-95(1996) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Strain: A3(2) / NRRL B-16638.
[3]	Matsumoto A., Hong S., Ishizuka H., Horinouchi S., Beppu T., Umeyama T. Submitted (APR-2001) to the EMBL/GenBank/DDBJ databases Cited for: SEQUENCE REVISION TO 239-240.
[4]	"Complete genome sequence of the model actinomycete Streptomyces coelicolor A3(2)." Bentley S.D., Chater K.F., Cerdeno-Tarraga A.-M., Challis G.L., Thomson N.R., James K.D., Harris D.E., Quail M.A., Kieser H., Harper D., Bateman A., Brown S., Chandra G., Chen C.W., Collins M., Cronin A., Fraser A., Goble A. , Hidalgo J., Hornsby T., Howarth S., Huang C.-H., Kieser T., Larke L., Murphy L.D., Oliver K., O'Neil S., Rabbinowitsch E., Rajandream M.A., Rutherford K.M., Rutter S., Seeger K., Saunders D., Sharp S., Squares R., Squares S., Taylor K., Warren T., Wietzorrek A., Woodward J.R., Barrell B.G., Parkhill J., Hopwood D.A. Nature 417:141-147(2002) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: ATCC BAA-471 / A3(2) / M145.
[5]	"Autophosphorylation of a bacterial serine/threonine kinase, AfsK, is inhibited by KbpA, an AfsK-binding protein." Umeyama T., Horinouchi S. J. Bacteriol. 183:5506-5512(2001) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH KBPA, AUTOPHOSPHORYLATION, MUTAGENESIS OF LYS-44.
[6]	"Self-activation of serine/threonine kinase AfsK on autophosphorylation at threonine-168." Tomono A., Mashiko M., Shimazu T., Inoue H., Nagasawa H., Yoshida M., Ohnishi Y., Horinouchi S. J. Antibiot. 59:117-123(2006) [PubMed] [Europe PMC] [Abstract] Cited for: AUTPOPHOSPHORYLATION AT SER-71 AND THR-168, MASS SPECTROMETRY, MUTAGENESIS OF SER-71; SER-128; THR-168 AND THR-170.

Cross-references

Sequence databases
EMBL GenBank DDBJ	D45382 Genomic DNA. Translation: BAA08229.2. AL939120 Genomic DNA. Translation: CAD55483.1.
RefSeq	NP_733637.1. NC_003888.3.
3D structure databases
ProteinModelPortal	P54741.
ModBase	Search...
Protein-protein interaction databases
STRING	100226.SCO4423.
PTM databases
PhosSite	P1007968.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
EnsemblBacteria	CAD55483; CAD55483; CAD55483.
GeneID	1099863.
KEGG	sco:SCO4423.
PATRIC	23738656. VBIStrCoe124346_4492.
Phylogenomic databases
eggNOG	COG0515.
HOGENOM	HOG000033839.
OMA	HGANPVE.
ProtClustDB	CLSK239456.
Enzyme and pathway databases
BRENDA	2.7.11.1. 5998.
Family and domain databases
InterPro	IPR011009. Kinase-like_dom. IPR018391. PQQ_beta_propeller_repeat. IPR002372. PQQ_repeat. IPR000719. Prot_kinase_cat_dom. IPR017441. Protein_kinase_ATP_BS. IPR011047. Quinonprotein_ADH-like_supfam. IPR008271. Ser/Thr_kinase_AS. [Graphical view]
Pfam	PF00069. Pkinase. 1 hit. PF01011. PQQ. 3 hits. [Graphical view]
SMART	SM00564. PQQ. 9 hits. [Graphical view]
SUPFAM	SSF56112. Kinase_like. 1 hit. SSF50998. Quin_alc_DH_like. 2 hits.
PROSITE	PS00107. PROTEIN_KINASE_ATP. 1 hit. PS50011. PROTEIN_KINASE_DOM. 1 hit. PS00108. PROTEIN_KINASE_ST. 1 hit. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AFSK_STRCO

Accession

Primary (citable) accession number: P54741
Secondary accession number(s): Q9F365, Q9L002

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	August 14, 2001
Last modified:	May 1, 2013
This is version 101 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Prokaryotic Protein Annotation Program